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Database: UniProt
Entry: B7MXY1_ECO81
LinkDB: B7MXY1_ECO81
Original site: B7MXY1_ECO81 
ID   B7MXY1_ECO81            Unreviewed;       120 AA.
AC   B7MXY1;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Dihydroneopterin triphosphate 2'-epimerase {ECO:0000256|ARBA:ARBA00044197};
DE            EC=5.1.99.7 {ECO:0000256|ARBA:ARBA00044039};
DE   AltName: Full=D-erythro-7,8-dihydroneopterin triphosphate epimerase {ECO:0000256|ARBA:ARBA00044306};
GN   Name=folX {ECO:0000313|EMBL:CAR08947.2};
GN   OrderedLocusNames=ECED1_2767 {ECO:0000313|EMBL:CAR08947.2};
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR08947.2, ECO:0000313|Proteomes:UP000000748};
RN   [1] {ECO:0000313|Proteomes:UP000000748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin
CC         3'-triphosphate; Xref=Rhea:RHEA:28346, ChEBI:CHEBI:58462,
CC         ChEBI:CHEBI:61186; EC=5.1.99.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00043806};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
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DR   EMBL; CU928162; CAR08947.2; -; Genomic_DNA.
DR   RefSeq; WP_000068457.1; NC_011745.1.
DR   AlphaFoldDB; B7MXY1; -.
DR   SMR; B7MXY1; -.
DR   GeneID; 75205651; -.
DR   KEGG; ecq:ECED1_2767; -.
DR   HOGENOM; CLU_112632_0_0_6; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR   GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd00534; DHNA_DHNTPE; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   InterPro; IPR006156; Dihydroneopterin_aldolase.
DR   InterPro; IPR006157; FolB_dom.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   NCBIfam; TIGR00526; folB_dom; 1.
DR   PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR42844:SF10; DIHYDRONEOPTERIN TRIPHOSPHATE 2'-EPIMERASE; 1.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   4: Predicted;
FT   DOMAIN          8..118
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   120 AA;  14082 MW;  5DDFF76540827ED6 CRC64;
     MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
     TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR
//
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